› 4d2o

X-ray diffraction
2.2Å resolution

Crystal structure of the class A extended-spectrum beta-lactamase PER- 2

Released:
DOI: 10.2210/pdb4d2o/pdb
PDB entry 4d2o coloured by chain, front view.
PDB entry 4d2o coloured by chain, side view.
PDB entry 4d2o coloured by chain, top view.
Source organism: Citrobacter freundii
Primary publication:
Crystal structure of the extended-spectrum β-lactamase PER-2 and insights into the role of specific residues in the interaction with β-lactams and β-lactamase inhibitors.
Ruggiero M, Kerff F, Herman R, Sapunaric F, Galleni M, Gutkind G, Charlier P, Sauvage E, Power P
Antimicrob Agents Chemother 58 5994-6002 (2014)
PMID: 25070104

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106954 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 284 amino acids
Theoretical weight: 30.96 KDa
Source organism: Citrobacter freundii
Expression system: Escherichia coli
UniProt:
  • Canonical: A2RP81 (Residues: 25-308; Coverage: 100%)
Gene name: blaPER-2
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 41.48Å b: 83.88Å c: 68.944Å
α: 90° β: 103.92° γ: 90°
R-values:
R R work R free
0.197 0.194 0.24
Expression system: Escherichia coli

Quick links

Citations

1 review citation

A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes.
Philippon et al. (2016)
5 other articles

7 mentions without citation

Exploring the Landscape of Diazabicyclooctane (DBO) Inhibition: Avibactam Inactivation of PER-2 β-Lactamase.
Ruggiero et al. (2017)
6 more